|
ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
|
| 言語種別 | 英語 |
| 発行・発表の年月 | 2008/03 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Crystal structure of the YdjC-family protein TTHB029 from Thermus thermophilus HB8: Structural relationship with peptidoglycan N-acetylglucosamine deacetylase |
| 執筆形態 | その他 |
| 掲載誌名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
| 出版社・発行元 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 巻・号・頁 | 367(3),pp.535-541 |
| 担当区分 | 最終著者,責任著者 |
| 著者・共著者 | Takahito Imagawa,Hitoshi Lino,Mayumi Kanagawa,Akio Ebihara,Seiki Kuramitsu,Hideaki Tsuge |
| 概要 | The YdjC-family protein is widely distributed, from human to bacteria, but so far no three-dimensional structure and functional analysis of this family of proteins has been reported. We determined the three-dimensional structure of the YdjC homolog TTHB029 at a resolution of 2.9 angstrom. The overall structure of the monomer consists of (beta alpha)-barrel fold forming a homodimer. Asp21, His60, and His127 residues coordinate to Mg2+ as a possible active site. TTHB029 shows structural similarity to the peptidoglycan N-acetylglucosamine deacetylase from Streptococcus pneumoniae (SpPgdA). The active site groove of SpPgdA includes the Zn2+ coordinated to Asp276, His326, and His330. Despite the low sequence identity, metal-binding residues of Asp-His-His were conserved among the two enzymes. There were definitive differences, however, in that one of the histidines of the metal-binding site was substituted for the other histidine located on the other loop. Moreover, these important metal-binding residues and the residues of the presumed active site are fully conserved in YdjC-family protein. (C) 2007 Elsevier Inc. All rights reserved. |
| DOI | 10.1016/j.bbrc.2007.12.144 |
| ISSN | 0006-291X |